The C-type lectin fold as an evolutionary solution for massive sequence variation

Nature Structural and Molecular Biology

Volumn 12, Issue 10, 2005, Pages 886-892

  McMahon, Stephen A ^a,d   Miller, Jason L ^a   Lawton, Jeffrey A ^a,e   Kerkow, Donald E ^a,f   Hodes, Asher ^b   Marti Renom, Marc A ^c   Doulatov, Sergei ^b,g   Narayanan, Eswar ^c   Sali, Andrej ^c   Miller, Jeff F ^b   Ghosh, Partho ^a  

^a UNIVERSITY OF CALIFORNIA   (United States)

^b UNIVERSITY OF CALIFORNIA   (United States)

^c UNIVERSITY OF CALIFORNIA   (United States)

^d UNIVERSITY OF ST ANDREWS   (United Kingdom)

^e EASTERN UNIVERSITY   (United States)

^f SCRIPPS RESEARCH INSTITUTE   (United States)

^g UNIVERSITY OF TORONTO   (Canada)

Author keywords

[No Author keywords available]

Indexed keywords

BINDING PROTEIN; IMMUNOGLOBULIN; LECTIN; PERTACTIN;

AMINO ACID SEQUENCE; ARTICLE; BACTERIOPHAGE; BINDING SITE; BORDETELLA; MOLECULAR EVOLUTION; NONHUMAN; PLANT GROWTH; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN BINDING; PROTEIN FOLDING; PROTEIN STABILITY; PROTEIN VARIANT; RECEPTOR BINDING; RETROPOSON;

AMINO ACID SEQUENCE; BACTERIAL OUTER MEMBRANE PROTEINS; BACTERIOPHAGES; BORDETELLA; EVOLUTION, MOLECULAR; GENOME, VIRAL; LECTINS, C-TYPE; MOLECULAR SEQUENCE DATA; PROTEIN CONFORMATION; PROTEIN FOLDING; VARIATION (GENETICS); VIRAL PROTEINS; VIRULENCE FACTORS, BORDETELLA;

BORDETELLA;

EID: 27144524301     PISSN: 15459993     EISSN: 15459985     Source Type: Journal    
DOI: 10.1038/nsmb992     Document Type: Article

References (36)

1. Liu, M. et al. Reverse transcriptase-mediated tropism switching in Bordetella bacteriophage. Science 295, 2091-2094 (2002).
2. Liu, M. et al. Genomic and genetic analysis of Bordetella bacteriophages encoding reverse transcriptase-mediated tropism-switching cassettes. J. Bacteriol. 186, 1503-1517 (2004).
3. Doulatov, S. et al. Tropism switching in Bordetella bacteriophage defines a family of diversity-generating retroelements. Nature 431, 476-481 (2004).
4. Chothia, C. & Lesk, A.M. Canonical structures for the hypervariable regions of immunoglobulins. J. Mol. Biol. 196, 901-917 (1987).
5. Davis, M.M. & Bjorkman, P.J. T-cell antigen receptor genes and T-cell recognition. Nature 334, 395-402 (1988).
6. Uhl, M.A. & Miller, J.F. Integration of multiple domains in a two-component sensor protein: the Bordetella pertussis BvgAS phosphorelay. EMBO J. 15, 1028-1036 (1996).
7. Akerley, B.J., Cotter, P.A. & Miller, J.F. Ectopic expression of the flagellar regulon alters development of the Bordetella-host interaction. Cell 80, 611-620 (1995).
8. Cotter, P.A. & Miller, J.F. A mutation in the Bordetella bronchiseptica bvgS gene results in reduced virulence and increased resistance to starvation, and identifies a new class of Bvg-regulated antigens. Mol. Microbiol. 24, 671-685 (1997).
9. Emsley, P., Charles, I.G., Fairweather, N.F. & Isaacs, N.W. Structure of Bordetella pertussis virulence factor P.69 pertactin. Nature 381, 90-92 (1996).
10. Hester, G., Kaku, H., Goldstein, I.J. & Wright, C.S. Structure of mannose-specific snowdrop (Galanthus nivalis) lectin is representative of a new plant lectin family. Nat. Struct. Biol. 2, 472-479 (1995).
11. Sauerborn, M.K., Wright, L.M., Reynolds, C.D., Grossmann, J.G. & Rizkallah, P.J. Insights into carbohydrate recognition by Narcissus pseudonarcissus lectin: the crystal structure at 2 A resolution in complex with alpha1-3 mannobiose. J. Mol. Biol. 290, 185-199 (1999).
12. Weis, W.I., Kahn, R., Fourme, R., Drickamer, K. & Hendrickson, W.A. Structure of the calcium-dependent lectin domain from a rat mannose-binding protein determined by MAD phasing. Science 254, 1608-1615 (1991).
13. Holm, L. & Sander, C. Protein structure comparison by alignment of distance matrices. J. Mol. Biol. 233, 123-138 (1993).
14. Feinberg, H. et al. Structure of a C-type carbohydrate recognition domain from the macrophage mannose receptor. J. Biol. Chem. 275, 21539-21548 (2000).
15. Batchelor, M. et al. Structural basis for recognition of the translocated intimin receptor (Tir) by intimin from enteropathogenic Escherichia coli. EMBO J. 19, 2452-2464 (2000).
16. Luo, Y. et al. Crystal structure of enteropathogenic Escherichia coli intimin-receptor complex. Nature 405, 1073-1077 (2000).
17. Drickamer, K. C-type lectin-like domains. Curr. Opin. Struct. Biol. 9, 585-590 (1999).
18. Tormo, J., Natarajan, K., Margulies, D.H. & Mariuzza, R.A. Crystal structure of a lectin-like natural killer cell receptor bound to its MHC class I ligand. Nature 402, 623-631 (1999).
19. Weis, W.I., Drickamer, K. & Hendrickson, W.A. Structure of a C-type mannose-binding protein complexed with an oligosaccharide. Nature 360, 127-134 (1992).
20. Takano, K., Yamagata, Y. & Yutani, K. A general rule for the relationship between hydrophobic effect and conformational stability of a protein: stability and structure of a series of hydrophobic mutants of human lysozyme. J. Mol. Biol. 280, 749-761 (1998).
21. Mooi, F.R. et al. Polymorphism in the Bordetella pertussis virulence factors P.69/pertactin and pertussis toxin in The Netherlands: temporal trends and evidence for vaccine-driven evolution. Infect. Immun. 66, 670-675 (1998).
22. Blum, M.L. et al. A structural motif in the variant surface glycoproteins of Trypanosoma brucei. Nature 362, 603-609 (1993).
23. Parge, H.E. et al. Structure of the fibre-forming protein pilin at 2.6 A resolution. Nature 378, 32-38 (1995).
24. Van der Ploeg, L.H. et al. An analysis of cosmid clones of nuclear DNA from Trypanosoma brucei shows that the genes for variant surface glycoproteins are clustered in the genome. Nucleic Acids Res. 10, 5905-5923 (1982).
25. Pancer, Z. et al. Somatic diversification of variable lymphocyte receptors in the agnathan sea lamprey. Nature 430, 174-180 (2004).
26. Bellotti, V., Mangione, P. & Merlini, G. Review: immunoglobulin light chain amyloidosis - the archetype of structural and pathogenic variability. J. Struct. Biol. 130, 280-289 (2000).
27. Stevens, F.J. Four structural risk factors identify most fibril-forming kappa light chains. Amyloid 7, 200-211 (2000).
28. Pokkuluri, P.R. et al. Increasing protein stability by polar surface residues: domain-wide consequences of interactions within a loop. Biophys. J. 82, 391-398 (2002).
29. Helms, L.R. & Wetzel, R. Destabilizing loop swaps in the CDRs of an immunoglobulin VL domain. Protein Sci. 4, 2073-2081 (1995).
30. Emsley, P., McDermott, G., Charles, I.G., Fairweather, N.F. & Isaacs, N.W. Crystallographic characterization of pertactin, a membrane-associated protein from Bordetella pertussis. J. Mol. Biol. 235, 772-773 (1994).
31. Otwinowski, Z. & Minor, W. Processing of x-ray diffraction data collected in oscillation mode. Methods Enzymol. 276, 307-326 (1997).
32. Terwilliger, T.C. Multiwavelength anomalous diffraction phasing of macromolecular structures: analysis of MAD data as single isomorphous replacement with anomalous scattering data using the MADMRG Program. Methods Enzymol. 276, 530-537 (1997).
33. Winn, M.D. An overview of the CCP4 project in protein crystallography: an example of a collaborative project. J. Synchrotron Radiat. 10, 23-25 (2003).
34. Perrakis, A. wARP: improvement and extension of crystallographic phases by weighted averaging of multiple-refined dummy atomic models. Acta Crystallogr. D Biol. Crystallogr. 53, 448-455 (1997).
35. Jones, T.A., Zou, J.-Y., Cowan, S.W. & Kjeldgaard, M. Improved methods for building protein models in electron density maps and the location of errors in these models. Acta Crystallogr. A 47, 110-119 (1991).
36. Wiseman, T., Williston, S., Brandts, J.F. & Lin, L.N. Rapid measurement of binding constants and heats of binding using a new titration calorimeter. Anal. Biochem. 179, 131-137 (1989).